HEXA1_DICDI
ID HEXA1_DICDI Reviewed; 532 AA.
AC P13723; Q54KX2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Beta-hexosaminidase subunit A1;
DE EC=3.2.1.52;
DE AltName: Full=Beta-N-acetylhexosaminidase subunit A1;
DE AltName: Full=N-acetyl-beta-glucosaminidase subunit A1;
DE Flags: Precursor;
GN Name=hexa1; Synonyms=nagA; ORFNames=DDB_G0287033;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 105-113; 260-276 AND
RP 295-306, FUNCTION, PTM, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=2972716; DOI=10.1016/s0021-9258(18)37465-9;
RA Graham T.R., Zassenhaus H.P., Kaplan A.;
RT "Molecular cloning of the cDNA which encodes beta-N-acetylhexosaminidase A
RT from Dictyostelium discoideum. Complete amino acid sequence and homology
RT with the human enzyme.";
RL J. Biol. Chem. 263:16823-16829(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP SUBUNIT.
RC STRAIN=NC-4;
RX PubMed=640375; DOI=10.1093/genetics/88.2.277;
RA Loomis W.F.;
RT "Genetic analysis of the gene for N-acetylglucosaminidase in Dictyostelium
RT discoideum.";
RL Genetics 88:277-284(1978).
CC -!- FUNCTION: Responsible for the degradation of GM2 gangliosides, and a
CC variety of other molecules containing terminal N-acetyl hexosamines.
CC This enzyme plays a role during the slug stage of development in the
CC maintenance of pseudoplasmodia of normal size.
CC {ECO:0000269|PubMed:2972716}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:640375}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:2972716}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:2972716}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR EMBL; J04065; AAA33230.1; -; mRNA.
DR EMBL; AAFI02000096; EAL63881.1; -; Genomic_DNA.
DR PIR; A30766; A30766.
DR RefSeq; XP_637398.1; XM_632306.1.
DR AlphaFoldDB; P13723; -.
DR SMR; P13723; -.
DR STRING; 44689.DDB0191256; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR PaxDb; P13723; -.
DR EnsemblProtists; EAL63881; EAL63881; DDB_G0287033.
DR GeneID; 8625929; -.
DR KEGG; ddi:DDB_G0287033; -.
DR dictyBase; DDB_G0287033; nagA.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_007082_0_4_1; -.
DR InParanoid; P13723; -.
DR OMA; QYWVDHA; -.
DR PhylomeDB; P13723; -.
DR Reactome; R-DDI-1660662; Glycosphingolipid metabolism.
DR Reactome; R-DDI-2022857; Keratan sulfate degradation.
DR Reactome; R-DDI-2024101; CS/DS degradation.
DR Reactome; R-DDI-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:P13723; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005764; C:lysosome; IDA:dictyBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:dictyBase.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR029019; HEX_eukaryotic_N.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF14845; Glycohydro_20b2; 1.
DR PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..532
FT /note="Beta-hexosaminidase subunit A1"
FT /id="PRO_0000012010"
FT ACT_SITE 308
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 532 AA; 59788 MW; CE651DD79F456514 CRC64;
MIKKIILFFA VLIAIVIGQQ PLNVVPYPQQ VSIGTCVIPV APGSILIESN IESATFSVSM
DRYTNLFFPF SNESEPSSNE SFLLSVTIYS DDETLQLGID ESYSLSIEQG SYQLKATNIY
GAMRGLETFK QLIVYNELEN SYSIVCVSIS DSPRYPWRGF MVDSARHYIP KNMILHMIDS
LGFSKFNTLH WHMVDAVAFP VESTTYPDLT KGAFSPSATF SHDDIQEVVA YAKTYGIRVI
PEFDIPGHAA AWGIGYPELV ATCPDYAANV NNIPLDISNP ATFTFIQNLF TEIAPLFIDN
YFHTGGDELV TGCWLEDPAI ANWMTKMGFS TTDAFQYFEN NLDVTMKSIN RTKITWNDPI
DYGVQLNPET LVQVWSSGSD LQGIVNSGYK ALVSFAWYLD KQNPDNNIHY EWQDTWQDFY
AADPTNNIST NAENIIGGEA TMWAEQINQV NWDVRVWPRA IGIAERLWSA QSVNSVSLAL
PRIGHFTCDL SRRGIQSGPL FPDYCPMQDD LVFTMKPNTK LSKSEIKLIL NK
